"Aprotinin" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
| Descriptor ID |
D007611
|
| MeSH Number(s) |
D12.776.083
|
| Concept/Terms |
Aprotinin- Aprotinin
- Trypsin Inhibitor, Basic, Pancreatic
- Bovine Kunitz Pancreatic Trypsin Inhibitor
- BPTI, Basic Pancreatic Trypsin Inhibitor
- Kallikrein-Trypsin Inactivator
- Inactivator, Kallikrein-Trypsin
- Kallikrein Trypsin Inactivator
- Kunitz Pancreatic Trypsin Inhibitor
- Trypsin Inhibitor, Kunitz, Pancreatic
- Basic Pancreatic Trypsin Inhibitor
- Bovine Pancreatic Trypsin Inhibitor
Contrykal- Contrykal
- Kontrykal
- Kontrikal
- Contrical
|
Below are MeSH descriptors whose meaning is more general than "Aprotinin".
Below are MeSH descriptors whose meaning is more specific than "Aprotinin".
This graph shows the total number of publications written about "Aprotinin" by people in this website by year, and whether "Aprotinin" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2004 | 0 | 1 | 1 |
| 2006 | 0 | 1 | 1 |
| 2007 | 1 | 0 | 1 |
| 2012 | 0 | 1 | 1 |
| 2017 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Aprotinin" by people in Profiles.
-
Gandhi JK, Manzar Z, Bachman LA, Andrews-Pfannkoch C, Knudsen T, Hill M, Schmidt H, Iezzi R, Pulido JS, Marmorstein AD. Fibrin hydrogels as a xenofree and rapidly degradable support for transplantation of retinal pigment epithelium monolayers. Acta Biomater. 2018 02; 67:134-146.
-
Newton PO, Bastrom TP, Emans JB, Shah SA, Shufflebarger HL, Sponseller PD, Sucato DJ, Lenke LG. Antifibrinolytic agents reduce blood loss during pediatric vertebral column resection procedures. Spine (Phila Pa 1976). 2012 Nov 01; 37(23):E1459-63.
-
Colwell CW, Chelly JE, Murkin JM, Stevens D, O'Keefe TJ, Hall R, Parvizi J. Randomized study of aprotinin effect on transfusions and blood loss in primary THA. Clin Orthop Relat Res. 2007 Dec; 465:189-95.
-
Mayer SA, Rincon F. Ultra-early hemostatic therapy for acute intracerebral hemorrhage. Semin Hematol. 2006 Jan; 43(1 Suppl 1):S70-6.
-
Rogers DM, Hirst JD. First-principles calculations of protein circular dichroism in the near ultraviolet. Biochemistry. 2004 Aug 31; 43(34):11092-102.
-
Feldman MD, Sataloff RT, Ballas SK. Autologous fibrin tissue adhesive for cerebrospinal fluid leaks: a controlled study of neurotoxicity. Am J Otol. 1988 Jul; 9(4):302-5.
-
Feldman MD, Sataloff RT, Choi HY, Ballas SK. Compatibility of autologous fibrin adhesive with implant materials. Arch Otolaryngol Head Neck Surg. 1988 Feb; 114(2):182-5.
-
Dejana E, Colella S, Languino LR, Balconi G, Corbascio GC, Marchisio PC. Fibrinogen induces adhesion, spreading, and microfilament organization of human endothelial cells in vitro. J Cell Biol. 1987 May; 104(5):1403-11.